Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus

Jian Wei Liu; Denis Verger; Paul D. Carr; Hong Yang; David L. Ollis

doi:10.1107/S0907444900005084

Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus

Jian Wei Liu, Denis Verger, Paul D. Carr, Hong Yang, David L. Ollis^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

2 Citations (Scopus)

Abstract

An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the α/β hydrolase fold. The crystals diffract to 2.8 Å and belong to space group I222 or 12₁2₁2₁, with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 Å.

Original language	English
Pages (from-to)	900-901
Number of pages	2
Journal	Acta Crystallographica Section D: Biological Crystallography
Volume	56
Issue number	7
DOIs	https://doi.org/10.1107/S0907444900005084
Publication status	Published - 2000

Access to Document

10.1107/S0907444900005084

Cite this

@article{46042aa876214ef3bf2207b5c880e66c,

title = "Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus",

abstract = "An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the α/β hydrolase fold. The crystals diffract to 2.8 {\AA} and belong to space group I222 or 1212121, with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 {\AA}.",

author = "Liu, {Jian Wei} and Denis Verger and Carr, {Paul D.} and Hong Yang and Ollis, {David L.}",

year = "2000",

doi = "10.1107/S0907444900005084",

language = "English",

volume = "56",

pages = "900--901",

journal = "Acta Crystallographica Section D: Biological Crystallography",

issn = "0907-4449",

publisher = "John Wiley & Sons Inc.",

number = "7",

}

TY - JOUR

T1 - Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus

AU - Liu, Jian Wei

AU - Verger, Denis

AU - Carr, Paul D.

AU - Yang, Hong

AU - Ollis, David L.

PY - 2000

Y1 - 2000

N2 - An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the α/β hydrolase fold. The crystals diffract to 2.8 Å and belong to space group I222 or 1212121, with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 Å.

AB - An esterase from the hyperthermophilic archeon Archaeoglobus fulgidus has been expressed, purified and crystallized in a form suitable for structure analysis. The enzyme has a molecular mass of 35 467 Da and shows sequence similarity to other esterases known to possess the α/β hydrolase fold. The crystals diffract to 2.8 Å and belong to space group I222 or 1212121, with unit-cell parameters a = 155.6, b = 155.0, c = 162.4 Å.

UR - http://www.scopus.com/inward/record.url?scp=0033949669&partnerID=8YFLogxK

U2 - 10.1107/S0907444900005084

DO - 10.1107/S0907444900005084

M3 - Article

SN - 0907-4449

VL - 56

SP - 900

EP - 901

JO - Acta Crystallographica Section D: Biological Crystallography

JF - Acta Crystallographica Section D: Biological Crystallography

IS - 7

ER -

Expression, purification and preliminary crystallographic studies of a hyperthermophilic esterase from Archaeoglobus fulgidus

Abstract

Access to Document

Other files and links

Fingerprint

Cite this